Protein precipitation and denaturation by dimethyl sulfoxide

Arakawa, Tsutomu; Kita, Yoshiko; Timasheff, Serge N.

doi:10.1016/j.bpc.2007.09.004

Cited by 284 publications

(259 citation statements)

References 54 publications

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“…Compared to glycerol, little is known about the DMSO-lysozyme interactions, apart from a preferential hydration of lysozyme in water-DMSO mixtures indicating a weak or no binding of DMSO to lysozyme. 3,4 This suggests that DMSO mainly influences the dielectric properties of the solution, and is consistent with the observed weaker temperature dependence of the cut-off length δ(T) in the case of DMSO.…”

Section: A Refractive Indices and Static Dielectric Constantssupporting

confidence: 83%

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Effect of glycerol and dimethyl sulfoxide on the phase behavior of lysozyme: Theory and experiments

Gögelein

Wagner

Cardinaux

et al. 2012

The Journal of Chemical Physics

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Salt, glycerol, and dimethyl sulfoxide (DMSO) are used to modify the properties of protein solutions. We experimentally determined the effect of these additives on the phase behavior of lysozyme solutions. Upon the addition of glycerol and DMSO, the fluid-solid transition and the gas-liquid coexistence curve (binodal) shift to lower temperatures and the gap between them increases. The experimentally observed trends are consistent with our theoretical predictions based on the thermodynamic perturbation theory and the Derjaguin-Landau-Verwey-Overbeek model for the lysozyme-lysozyme pair interactions. The values of the parameters describing the interactions, namely the refractive indices, dielectric constants, Hamaker constant and cut-off length, are extracted from literature or are experimentally determined by independent experiments, including static light scattering, to determine the second virial coefficient. We observe that both, glycerol and DMSO, render the potential more repulsive, while sodium chloride reduces the repulsion.

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Section: A Refractive Indices and Static Dielectric Constantssupporting

confidence: 83%

“…Similar observations were made by Kulkarni and Zukoski. 26 Furthermore, Arakawa et al 3 and Kamiyama et al 4 observed a preferential hydration of lysozyme in water-DMSO mixtures, indicating that DMSO does not bind to the lysozyme surface. 4 This suggests that DMSO mainly affects the dielectric properties of the bulk solution.…”

Section: Introductionmentioning

confidence: 99%

Effect of glycerol and dimethyl sulfoxide on the phase behavior of lysozyme: Theory and experiments

Gögelein

Wagner

Cardinaux

et al. 2012

The Journal of Chemical Physics

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“…4,5,11 The characteristics shown for this H-bond suggest that NMF might be more strongly H-bonded to DMSO than to water, or, if DMSO is added as co-solute to an aqueous solution of NMF, the water molecules H-bonded to the amine hydrogen would be delocated for it, in line with results reported previously. 9,11 Besides the O(DMSO)-H(NMF) H-bond, the results point to a secondary auxiliary S-HN H-bond, what must collaborate for the structure of the mixture.…”

Section: Discussionmentioning

confidence: 95%

“…4,5 It has been shown that at moderate concentrations DMSO enhances enzyme activity (behaves as a kosmotropic agent) by increasing the conformational flexibility of the protein, 6,7 while in other cases the protein functionality was decreased (DMSO behaves as a chaotropic agent) by enhancing the protein rigidity. 8,9 Proteins dissolved in pure DMSO cannot exhibit functional activity because they become unable to adopt the native structure. 10 Experimental results suggest that DMSO denatures folded proteins by excluding water molecules from the protein surface.…”

Section: Introductionmentioning

confidence: 99%

A hybrid neutron diffraction and computer simulation study on the solvation of N-methylformamide in dimethylsulfoxide

Cordeiro

Soper²

2013

The Journal of Chemical Physics

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Articles you may be interested inThe solvation of N-methylformamide (NMF) by dimethylsulfoxide (DMSO) in a 20% NMF/DMSO liquid mixture is investigated using a combination of neutron diffraction augmented with isotopic substitution and Monte Carlo simulations. The aim is to investigate the solute-solvent interactions and the structure of the solution. The results point to the formation of a hydrogen bond (H-bond) between the H bonded to the N of the amine group of NMF and the O of DMSO particularly strong when compared with other H-bonded liquids. Moreover, a second cooperative H-bond is identified with the S atom of DMSO. As a consequence of these H-bonds, molecules of NMF and DMSO are rather rigidly connected, establishing very stable dimmers in the mixture and very well organized first and second solvation shells.

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“…For this method we selected DMSO as the component of lysis buffer because of being a polar-aprotic solvent (Wang et al 2008;Di and Kerns 2006). Lipids and proteins have limited solubility in DMSO, which removes proteins through its denaturing and precipitating action and also inhibits the activity of nucleases (Arakawa et al 2007), which helps reduce false DNA fragmentation during sample processing. In addition, DMSO is known to inhibit the formation of folded DNA structure (Kang et al 2005), which results in increased band intensity on the agarose gel following staining with fluorochromes such as ethidium bromide.…”

Section: Resultsmentioning

confidence: 99%

An improved non-enzymatic “DNA ladder assay” for more sensitive and early detection of apoptosis

2011

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Conventional DNA ladder assay has certain shortcomings such as loss of DNA fragments during sample processing, involvement of multiple steps and requirement of expensive reagents. The present study demonstrates a rapid, easy-to-perform cost-effective method for detection of apoptotic DNA fragments with considerable improvement in the sensitivity by avoiding loss of DNA fragments. It involves a few minutes of procedure involving direct lysis of cells with dimethyl sulphoxide (DMSO), brief vortexing, addition of 2% SDS-TE buffer, and a single step of centrifugation. This cost-and time-efficient method reduces the assay time considerably and can be used for a large number of samples with excellent sensitivity.

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Protein precipitation and denaturation by dimethyl sulfoxide

Cited by 284 publications

References 54 publications

Effect of glycerol and dimethyl sulfoxide on the phase behavior of lysozyme: Theory and experiments

Effect of glycerol and dimethyl sulfoxide on the phase behavior of lysozyme: Theory and experiments

A hybrid neutron diffraction and computer simulation study on the solvation of N-methylformamide in dimethylsulfoxide

An improved non-enzymatic “DNA ladder assay” for more sensitive and early detection of apoptosis

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